Production of alkenes and novel secondary products by P450 OleTJE using novel H2O2-generating fusion protein systems
Matthews, Sarah and Tee, Kang Lan and Rattray, Nicholas J. and McLean, Kirsty J. and Leys, David and Parker, David A. and Blankley, Richard T. and Munro, Andrew W. (2017) Production of alkenes and novel secondary products by P450 OleTJE using novel H2O2-generating fusion protein systems. FEBS Letters, 591 (5). pp. 737-750. ISSN 0014-5793 (https://doi.org/10.1002/1873-3468.12581)
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Abstract
Jeotgalicoccus sp. 8456 OleTJE (CYP152L1) is a fatty acid decarboxylase cytochrome P450 that uses hydrogen peroxide (H2O2) to catalyse production of terminal alkenes, which are industrially important chemicals with biofuel applications. We report enzyme fusion systems in which Streptomyces coelicolor alditol oxidase (AldO) is linked to OleTJE. AldO oxidizes polyols (including glycerol), generating H2O2 as a coproduct and facilitating its use for efficient OleTJE-dependent fatty acid decarboxylation. AldO activity is regulatable by polyol substrate titration, enabling control over H2O2 supply to minimize oxidative inactivation of OleTJE and prolong activity for increased alkene production. We also use these fusion systems to generate novel products from secondary turnover of 2-OH and 3-OH myristic acid primary products, expanding the catalytic repertoire of OleTJE.
ORCID iDs
Matthews, Sarah, Tee, Kang Lan, Rattray, Nicholas J. ORCID: https://orcid.org/0000-0002-3528-6905, McLean, Kirsty J., Leys, David, Parker, David A., Blankley, Richard T. and Munro, Andrew W.;-
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Item type: Article ID code: 77526 Dates: DateEvent31 March 2017Published1 February 2017Published Online26 January 2017AcceptedSubjects: Science > Natural history > Biology Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences Depositing user: Pure Administrator Date deposited: 24 Aug 2021 09:41 Last modified: 11 Nov 2024 13:12 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/77526